ID   A0A259BG01_9GAMM        Unreviewed;       627 AA.
AC   A0A259BG01;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE   AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN   Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN   ORFNames=B7Y07_00170 {ECO:0000313|EMBL:OYZ88386.1};
OS   Halothiobacillus sp. 24-54-40.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=1970385 {ECO:0000313|EMBL:OYZ88386.1, ECO:0000313|Proteomes:UP000215882};
RN   [1] {ECO:0000313|EMBL:OYZ88386.1, ECO:0000313|Proteomes:UP000215882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=24-54-40 {ECO:0000313|EMBL:OYZ88386.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_00505}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYZ88386.1}.
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DR   EMBL; NCHR01000001; OYZ88386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259BG01; -.
DR   EnsemblBacteria; OYZ88386; OYZ88386; B7Y07_00170.
DR   Proteomes; UP000215882; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   HAMAP; MF_00505; HSP90; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00505};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00505}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT   DOMAIN          27..184
FT                   /note="Histidine kinase/HSP90-like ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00387"
FT   REGION          1..343
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT   REGION          557..627
FT                   /note="C"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   627 AA;  70436 MW;  4B20B6B18ECCE84E CRC64;
     MSQPEIRGFQ TEVKELLQLM IHSLYSNPEI FLRELVSNAS DACDKLRFEA VSDDALYEGD
     ETLRIRVSFD AAAKTVTISD NGIGMNRDEV IENIGTIARS GTKAFIQKLG QDQAKDLSQI
     GQFGVGFYSA FIVAEEVVLT TRRAGMGSEH GVRWTSRGEG EYALETVDSA ERGTSIVLKL
     REDHADFADD WRLRSVIRKY SDHITFPIEM VKAPSPAMDD EEAAAPEVPS WERINDATAL
     WVRPKSAISD EEYTEFYKHV GHDWEAPLAW SHNRVEGKTE YTSLLYLPAR APFDLWDRET
     KQGIKLYVKR VFIMDDAEKL MPRYLRFVRG VIDSADLPLN VSREILQSNR VLDTIRQGSV
     KRILGMLEQM AANEPEKYAK FWGTFGQVLK EGVGEDFANR EQIAGLLRFA STHTGNDTPS
     VSFKDAIDRL PEGQEEIYYI IADSYAAALA SPHLEIFRKK GIEVLLLSDR IDEWLMSQLT
     EFSGKKLKSV TRAEVSLDDA AEESTPDAKE AQSALVERLK KVLTELVDDV RVSKRLVDSP
     ACLVTTEEEM SLHLQRLLKE AGQAAPTVKP ILEINPQHPL LQRAEAESDE ARFEDIARVL
     LGQATLAEGG HLTEAADFVL RLNRLLV
//